Albert S. Mildvan

1.0k total citations
19 papers, 886 citations indexed

About

Albert S. Mildvan is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Albert S. Mildvan has authored 19 papers receiving a total of 886 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Materials Chemistry and 5 papers in Organic Chemistry. Recurrent topics in Albert S. Mildvan's work include Enzyme Structure and Function (8 papers), RNA and protein synthesis mechanisms (5 papers) and Biochemical and Molecular Research (4 papers). Albert S. Mildvan is often cited by papers focused on Enzyme Structure and Function (8 papers), RNA and protein synthesis mechanisms (5 papers) and Biochemical and Molecular Research (4 papers). Albert S. Mildvan collaborates with scholars based in United States, France and Japan. Albert S. Mildvan's co-authors include Athan Kuliopulos, David J. Weber, Paul Talalay, Chitrananda Abeygunawardana, Ravindra Kumar Gupta, David Shortle, Christian P. Whitman, James T. Stivers, Thomas M. Li and Robert L. Switzer and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Annual Review of Biochemistry.

In The Last Decade

Albert S. Mildvan

19 papers receiving 818 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Albert S. Mildvan United States 13 622 218 121 90 81 19 886
Robert Delaney United States 15 504 0.8× 142 0.7× 56 0.5× 73 0.8× 32 0.4× 30 1.0k
Ahmad Salahuddin India 16 702 1.1× 210 1.0× 104 0.9× 99 1.1× 26 0.3× 76 1.0k
Ewa Ciszak United States 14 618 1.0× 224 1.0× 90 0.7× 80 0.9× 82 1.0× 30 927
H.-S. Shieh United States 16 644 1.0× 186 0.9× 256 2.1× 99 1.1× 194 2.4× 28 1.2k
Paulus A. Kroon United States 25 856 1.4× 62 0.3× 137 1.1× 133 1.5× 218 2.7× 42 1.6k
Jill R. Cupp‐Vickery United States 17 883 1.4× 219 1.0× 51 0.4× 107 1.2× 53 0.7× 23 1.5k
David P. Ringer United States 20 803 1.3× 102 0.5× 77 0.6× 119 1.3× 38 0.5× 58 1.1k
William J. Metzler United States 22 900 1.4× 273 1.3× 140 1.2× 217 2.4× 105 1.3× 45 1.4k
Gustaf Söderlund Sweden 6 706 1.1× 273 1.3× 60 0.5× 79 0.9× 64 0.8× 7 1.2k
Grayson H. Snyder United States 16 689 1.1× 156 0.7× 89 0.7× 196 2.2× 30 0.4× 18 924

Countries citing papers authored by Albert S. Mildvan

Since Specialization
Citations

This map shows the geographic impact of Albert S. Mildvan's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Albert S. Mildvan with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Albert S. Mildvan more than expected).

Fields of papers citing papers by Albert S. Mildvan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Albert S. Mildvan. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Albert S. Mildvan. The network helps show where Albert S. Mildvan may publish in the future.

Co-authorship network of co-authors of Albert S. Mildvan

This figure shows the co-authorship network connecting the top 25 collaborators of Albert S. Mildvan. A scholar is included among the top collaborators of Albert S. Mildvan based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Albert S. Mildvan. Albert S. Mildvan is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

19 of 19 papers shown
1.
Stivers, James T., Chitrananda Abeygunawardana, Christian P. Whitman, & Albert S. Mildvan. (1996). 4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy. Protein Science. 5(4). 729–741. 17 indexed citations
2.
Stivers, James T., et al.. (1996). 4-Oxalocrotonate Tautomerase:  pH Dependence of Catalysis and pKa Values of Active Site Residues. Biochemistry. 35(3). 814–823. 90 indexed citations
3.
Abeygunawardana, Chitrananda, David J. Weber, Apostolos G. Gittis, et al.. (1995). Solution Structure of the MutT Enzyme, a Nucleoside Triphosphate Pyrophosphohydrolase. Biochemistry. 34(46). 14997–15005. 71 indexed citations
4.
Weber, David J., et al.. (1994). NMR Docking of a Substrate into the X-ray Structure of the Asp-21 .fwdarw. Glu Mutant of Staphylococcal Nuclease. Biochemistry. 33(26). 8017–8028. 7 indexed citations
5.
Chuang, Woei‐Jer, Apostolos G. Gittis, & Albert S. Mildvan. (1994). Magnetic resonance studies of the binding of oligonucleotide substrates to mutants of staphylococcal nuclease. Proteins Structure Function and Bioinformatics. 18(1). 68–80. 1 indexed citations
6.
Chuang, Woei‐Jer, David J. Weber, Apostolos G. Gittis, & Albert S. Mildvan. (1993). Mutational tests of the NMR‐docked structure of the staphylococcal nuclease–metal–3′,5′‐pdTp complex. Proteins Structure Function and Bioinformatics. 17(1). 36–48. 4 indexed citations
7.
Martı́nez, Aurora, Chitrananda Abeygunawardana, Jan Haavik, Torgeir Flatmark, & Albert S. Mildvan. (1993). Interaction of Substrate and Pterin Cofactor with the Metal of Human Tyrosine Hydroxylase as Determined by 1H-NMR. Advances in experimental medicine and biology. 338. 77–80. 9 indexed citations
8.
Mildvan, Albert S., David J. Weber, & Athan Kuliopulos. (1992). Quantitative interpretations of double mutations of enzymes. Archives of Biochemistry and Biophysics. 294(2). 327–340. 131 indexed citations
9.
Weber, David J., et al.. (1991). Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR. Biochemistry. 30(30). 7425–7437. 30 indexed citations
10.
Kuliopulos, Athan, Paul Talalay, & Albert S. Mildvan. (1990). Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction. Biochemistry. 29(44). 10271–10280. 51 indexed citations
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Kuliopulos, Athan, Albert S. Mildvan, David Shortle, & Paul Talalay. (1989). Kinetic and ultraviolet spectroscopic studies of active-site mutants of .DELTA.5-3-ketosteroid isomerase. Biochemistry. 28(1). 149–159. 110 indexed citations
14.
Rosevear, Paul R., et al.. (1987). Nuclear Overhauser effect studies on the conformation of magnesium adenosine 5'-triphosphate bound to rabbit muscle creatine kinase. Biochemistry. 26(17). 5338–5344. 18 indexed citations
15.
Mincey, Terry, et al.. (1980). Presence of a flavin semiquinone in methanol oxidase.. Proceedings of the National Academy of Sciences. 77(12). 7099–7101. 26 indexed citations
16.
Li, Thomas M., Albert S. Mildvan, & Robert L. Switzer. (1978). Studies of the stereochemistry and of the role of metal ions in the mechanism of phosphoribosylpyrophosphate synthetase from Salmonella typhimurium.. Journal of Biological Chemistry. 253(11). 3918–3923. 61 indexed citations
17.
Ray, William J., Albert S. Mildvan, & John B. Grutzner. (1977). Phosphorus nuclear magnetic resonance studies of phosphoglucomutase and its metal ion complexes. Archives of Biochemistry and Biophysics. 184(2). 453–463. 12 indexed citations
18.
19.
Mildvan, Albert S.. (1974). Mechanism of Enzyme Action. Annual Review of Biochemistry. 43(1). 357–399. 130 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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